UniProt Accession

 NRIP1_HUMAN; P48552; Q8IWE8 

Genbank Protein ID

 X84373; AF248484; AF127577; AL163207; BC040361 

Genbank Nucleotide ID

 CAA59108.1; AAF62185.1; AAF35255.1; CAB90396.1; AAH40361.1 

Protein Name

 Nuclear receptor-interacting protein 1 

Protein Synonyms/Alias

 Nuclear factor RIP140; Receptor-interacting protein 140 

Gene Name

 NRIP1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
97	SEDWNAAKRKRLSDS	ubiquitination	[1]
111	SIMNLNVKKEALLAG	acetylation	[2]
158	QQIRQSLKEQGYALS	acetylation	[2]
170	ALSHDSLKVEKDLRC	sumoylation	[3]
286	YSREHALKTQNANQA	acetylation	[2]
286	YSREHALKTQNANQA	ubiquitination	[1]
310	RLQENGQKDVGSYQL	acetylation	[2]
446	VPIDLSCKHRTEKSE	acetylation	[2, 4]
481	KVPDVDIKEDQDTSK	acetylation	[2]
590	VCSTQSEKLTNTASN	methylation	[5]
652	VEEQRPSKQLLTGNT	methylation	[5]
677	NSPLLSNKTNAVEEN	ubiquitination	[1]
756	QILMVKIKSEPCDDL	methylation	[5]
756	QILMVKIKSEPCDDL	sumoylation	[3]
963	SVADSKKKGHKNNVT	acetylation	[6]
966	DSKKKGHKNNVTNSK	acetylation	[6]
1105	SVSQVTAKEELLPTA	ubiquitination	[1]
1115	LLPTAETKASFFNLR	ubiquitination	[7, 8]
1154	LGSVLTIKKESE***	sumoylation	[3]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
 [3] SUMOylation modulates the transcription repressor function of RIP140.
 Rytinki MM, Palvimo JJ.
 J Biol Chem. 2008 Apr 25;283(17):11586-95. [PMID: 18211901]
 [4] Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP.
 Vo N, Fjeld C, Goodman RH.
 Mol Cell Biol. 2001 Sep;21(18):6181-8. [PMID: 11509661]
 [5] Lysine methylation of nuclear co-repressor receptor interacting protein 140.
 Huq MD, Ha SG, Barcelona H, Wei LN.
 J Proteome Res. 2009 Mar;8(3):1156-67. [PMID: 19216533]
 [6] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 Modulates transcriptional activation by steroid receptors such as NR3C1, NR3C2 and ESR1. Also modulates transcriptional repression by nuclear hormone receptors. 

Sequence Annotation

 REGION 1 415 Interaction with ZNF366.
 REGION 78 333 Repression domain 1.
 REGION 410 700 Repression domain 2.
 REGION 431 472 Required for targeting to small nuclear
 REGION 735 885 Repression domain 3.
 REGION 753 1158 Interaction with ZNF366.
 REGION 1118 1158 Repression domain 4.
 MOTIF 21 25 LXXLL motif 1.
 MOTIF 133 137 LXXLL motif 2.
 MOTIF 185 189 LXXLL motif 3.
 MOTIF 266 270 LXXLL motif 4.
 MOTIF 380 384 LXXLL motif 5.
 MOTIF 440 446 CTBP-binding; principal site.
 MOTIF 500 504 LXXLL motif 6.
 MOTIF 565 569 CTBP-binding.
 MOTIF 599 603 CTBP-binding (Potential).
 MOTIF 713 717 LXXLL motif 7.
 MOTIF 819 823 LXXLL motif 8.
 MOTIF 936 940 LXXLL motif 9.
 MOTIF 946 950 CTBP-binding.
 MOTIF 1061 1074 Ligand-dependent nuclear receptor binding
 MOD_RES 104 104 Phosphoserine (By similarity).
 MOD_RES 111 111 N6-acetyllysine (By similarity).
 MOD_RES 158 158 N6-acetyllysine (By similarity).
 MOD_RES 207 207 Phosphothreonine (By similarity).
 MOD_RES 286 286 N6-acetyllysine (By similarity).
 MOD_RES 310 310 N6-acetyllysine (By similarity).
 MOD_RES 356 356 Phosphoserine (By similarity).
 MOD_RES 378 378 Phosphoserine (By similarity).
 MOD_RES 446 446 N6-acetyllysine.
 MOD_RES 481 481 N6-acetyllysine (By similarity).
 MOD_RES 487 487 Phosphoserine (By similarity).
 MOD_RES 518 518 Phosphoserine (By similarity).
 MOD_RES 528 528 N6-acetyllysine (By similarity).
 MOD_RES 542 542 Phosphoserine (By similarity).
 MOD_RES 606 606 N6-acetyllysine (By similarity).
 MOD_RES 671 671 Phosphoserine (By similarity).
 MOD_RES 931 931 N6-acetyllysine (By similarity).
 MOD_RES 1001 1001 Phosphoserine (By similarity).  

Keyword

 3D-structure; Acetylation; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1158 AA 

Protein Sequence

Gene Ontology

 GO:0000118; C:histone deacetylase complex; IEA:Compara.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
 GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
 GO:0019915; P:lipid storage; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0001543; P:ovarian follicle rupture; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

Interpro

 IPR026649; NRIP1. 

Pfam

  

SMART

  

PROSITE

  

PRINTS